Experimental porphyria produced by chlorinated hydrocarbons. Studies on porphyrinogen carboxylase in the experiment model of human porphyria cutanea tarda

The present work tries to elucidate if the strong decrease of porphyrinogen carboxylase (PCL) observed in experimental porphyria caused by hexachlorobenzene (HCB) is due to the presence of an inhibitor or to a modification of the protein structure of the enzyme. For this purpose: a) cross-assays and...

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Autores principales:	Ríos de Molina, María del Carmen, Billi de Catabbi, Silvia Cristina, Wainstok de Calmanovici, Rosa, San Martín de Viale, Leonor Carmen
Publicado:	1984
Materias:	chlorinated hydrocarbon hexachlorobenzene uroporphyrinogen decarboxylase animal experiment enzyme inhibition human intoxication porphyria cutanea tarda rat Animal Carboxy-Lyases Disease Models, Animal English Abstract Female Heat Hexachlorobenzene Liver Porphyria Rats Rats, Inbred Strains Skin Diseases
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00016764_v34_n4_p393_RiosdeMolina http://hdl.handle.net/20.500.12110/paper_00016764_v34_n4_p393_RiosdeMolina
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_00016764_v34_n4_p393_RiosdeMolina
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spelling	paper:paper_00016764_v34_n4_p393_RiosdeMolina2025-07-30T17:05:25Z Experimental porphyria produced by chlorinated hydrocarbons. Studies on porphyrinogen carboxylase in the experiment model of human porphyria cutanea tarda Ríos de Molina, María del Carmen Billi de Catabbi, Silvia Cristina Wainstok de Calmanovici, Rosa San Martín de Viale, Leonor Carmen chlorinated hydrocarbon hexachlorobenzene uroporphyrinogen decarboxylase animal experiment enzyme inhibition human intoxication porphyria cutanea tarda rat Animal Carboxy-Lyases Disease Models, Animal English Abstract Female Heat Hexachlorobenzene Liver Porphyria Rats Rats, Inbred Strains Skin Diseases The present work tries to elucidate if the strong decrease of porphyrinogen carboxylase (PCL) observed in experimental porphyria caused by hexachlorobenzene (HCB) is due to the presence of an inhibitor or to a modification of the protein structure of the enzyme. For this purpose: a) cross-assays and heating ones were performed in order to look for the existence of a compound, that present in porphyric animals, would be responsible for the decrease of PCL activity found in them; b) the effect in vitro of HCB, HCB metabolites and other related compounds was studied to find the inhibitor of PCL activity and to look for a structure-inhibitory effect relation, c) hepatic PCL from porphyric and normal rats was purified, and enzyme properties were comparatively studied looking for structural differences between the enzymes obtained from both animal lots. The results indicate that: a) the heat deproteinized porphyric liver preparation produces an inhibition on the normal preparation, but it is smaller than the decrease produced in vivo by the HCB on this enzyme activity; thus other reasons may explain this behavior of PCL in intoxicated animals: b) the HCB had no effect on PCL activity; the phenolic compounds exhibited inhibitions of variable extent that were increased by the presence of electrophilic substituents. Fil:Rios de Molina, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Billi, S.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Wainstok de Calmanovici, R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:San Martin de Viale, L.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1984 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00016764_v34_n4_p393_RiosdeMolina http://hdl.handle.net/20.500.12110/paper_00016764_v34_n4_p393_RiosdeMolina
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	chlorinated hydrocarbon hexachlorobenzene uroporphyrinogen decarboxylase animal experiment enzyme inhibition human intoxication porphyria cutanea tarda rat Animal Carboxy-Lyases Disease Models, Animal English Abstract Female Heat Hexachlorobenzene Liver Porphyria Rats Rats, Inbred Strains Skin Diseases
spellingShingle	chlorinated hydrocarbon hexachlorobenzene uroporphyrinogen decarboxylase animal experiment enzyme inhibition human intoxication porphyria cutanea tarda rat Animal Carboxy-Lyases Disease Models, Animal English Abstract Female Heat Hexachlorobenzene Liver Porphyria Rats Rats, Inbred Strains Skin Diseases Ríos de Molina, María del Carmen Billi de Catabbi, Silvia Cristina Wainstok de Calmanovici, Rosa San Martín de Viale, Leonor Carmen Experimental porphyria produced by chlorinated hydrocarbons. Studies on porphyrinogen carboxylase in the experiment model of human porphyria cutanea tarda
topic_facet	chlorinated hydrocarbon hexachlorobenzene uroporphyrinogen decarboxylase animal experiment enzyme inhibition human intoxication porphyria cutanea tarda rat Animal Carboxy-Lyases Disease Models, Animal English Abstract Female Heat Hexachlorobenzene Liver Porphyria Rats Rats, Inbred Strains Skin Diseases
description	The present work tries to elucidate if the strong decrease of porphyrinogen carboxylase (PCL) observed in experimental porphyria caused by hexachlorobenzene (HCB) is due to the presence of an inhibitor or to a modification of the protein structure of the enzyme. For this purpose: a) cross-assays and heating ones were performed in order to look for the existence of a compound, that present in porphyric animals, would be responsible for the decrease of PCL activity found in them; b) the effect in vitro of HCB, HCB metabolites and other related compounds was studied to find the inhibitor of PCL activity and to look for a structure-inhibitory effect relation, c) hepatic PCL from porphyric and normal rats was purified, and enzyme properties were comparatively studied looking for structural differences between the enzymes obtained from both animal lots. The results indicate that: a) the heat deproteinized porphyric liver preparation produces an inhibition on the normal preparation, but it is smaller than the decrease produced in vivo by the HCB on this enzyme activity; thus other reasons may explain this behavior of PCL in intoxicated animals: b) the HCB had no effect on PCL activity; the phenolic compounds exhibited inhibitions of variable extent that were increased by the presence of electrophilic substituents.
author	Ríos de Molina, María del Carmen Billi de Catabbi, Silvia Cristina Wainstok de Calmanovici, Rosa San Martín de Viale, Leonor Carmen
author_facet	Ríos de Molina, María del Carmen Billi de Catabbi, Silvia Cristina Wainstok de Calmanovici, Rosa San Martín de Viale, Leonor Carmen
author_sort	Ríos de Molina, María del Carmen
title	Experimental porphyria produced by chlorinated hydrocarbons. Studies on porphyrinogen carboxylase in the experiment model of human porphyria cutanea tarda
title_short	Experimental porphyria produced by chlorinated hydrocarbons. Studies on porphyrinogen carboxylase in the experiment model of human porphyria cutanea tarda
title_full	Experimental porphyria produced by chlorinated hydrocarbons. Studies on porphyrinogen carboxylase in the experiment model of human porphyria cutanea tarda
title_fullStr	Experimental porphyria produced by chlorinated hydrocarbons. Studies on porphyrinogen carboxylase in the experiment model of human porphyria cutanea tarda
title_full_unstemmed	Experimental porphyria produced by chlorinated hydrocarbons. Studies on porphyrinogen carboxylase in the experiment model of human porphyria cutanea tarda
title_sort	experimental porphyria produced by chlorinated hydrocarbons. studies on porphyrinogen carboxylase in the experiment model of human porphyria cutanea tarda
publishDate	1984
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00016764_v34_n4_p393_RiosdeMolina http://hdl.handle.net/20.500.12110/paper_00016764_v34_n4_p393_RiosdeMolina
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Experimental porphyria produced by chlorinated hydrocarbons. Studies on porphyrinogen carboxylase in the experiment model of human porphyria cutanea tarda

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